Kinetic properties of N6-(2-carboxyethyl)-NAD(H) and poly(ethylene glycol)-bound NAD(H) for alcohol, lactate, malate and glyceraldehyde-3-phosphate dehydrogenase from different organisms

• Published in: Enzyme and microbial technology Vol. 6; no. 12; pp. 538 - 542
• Main Authors: Katayama, Nozomi, Hayakawa, Ken, Urabe, Itaru, Okada, Hirosuke
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier Inc 01.12.1984; Elsevier Science
• Subjects: alcohol dehydrogenase; Analytical, structural and metabolic biochemistry; Biological and medical sciences; Biology of microorganisms of confirmed or potential industrial interest; Biotechnology; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; glyceraldehyde-3-phosphate dehydrogenase; Kinetics; lactate dehydrogenase; malate dehydrogenase; Mission oriented research; N6-(2-carboxyethyl)-NAD(H); Oxidoreductases; Physiology and metabolism; poly(ethylene glycol)-bound NAD(H); poly(ethylene glycol)-bound NAD(H); lactate dehydrogenase; N 6-(2-carboxyethyl)-NAD(H); alcohol dehydrogenase; Kinetics; glyceraldehyde-3-phosphate dehydrogenase; malate dehydrogenase; NADH; Enzyme; Glyceraldehyde-phosphate dehydrogenase; Bacteria; Lactate dehydrogenase; Malate dehydrogenase; Alcohol dehydrogenase; Coenzyme; Biological constant
• ISSN: 0141-0229; 1879-0909
• DOI: 10.1016/0141-0229(84)90082-6

The steady-state kinetics of alcohol dehydrogenases (alcohol:NAD + oxidoreductase, EC 1.1.1.1 and alcohol:NADP + oxidoreductase, EC 1.1.1.2), lactate dehydrogenases ( l-lactate:NAD + oxidoreductase, EC 1.1.1.27 and d-lactate:NAD + oxidoreductase, EC 1.1.1.28), malate dehydrogenase ( l-malate:NAD + oxidoreductase, EC 1.1.1.37), and glyceraldehyde-3-phosphate dehydrogenases [ d-glyceraldehyde-3-phosphate:NAD + oxidoreductase (phosphorylating), EC 1.2.1.12] from different sources (prokaryote and eukaryote, mesophilic and thermophilic organisms) have been studied using NAD(H), N 6-(2-carboxyethyl)-NAD(H), and poly(ethylene glycol)-bound NAD(H) as coenzymes. The kinetic constants for NAD(H) were changed by carboxyethylation of the 6-amino group of the adenine ring and by conversion to macromolecular form. Enzymes from thermophilic bacteria showed especially high activities for the derivatives. The relative values of the maximum velocity ( NAD = 1) of Thermus thermophilus malate dehydrogenase for N 6-(2-carboxyethyl)-NAD and poly(ethylene glycol)-bound NAD were 5.7 and 1.9, respectively, and that of Bacillus stearothermophilus glyceraldehyde-3-phosphate dehydrogenase for poly(ethylene glycol)-bound NAD was 1.9.